First-pass extracted concept

heparan sulfate-mediated PFV attachment

Candidate: concept label1 source documents3 linked claims

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Aliases

HS-mediated attachment, PFV Env-HS interactions

Evidence Snippets

Alanine substitutions at R298, R440, and E446 in the UD abolished infectivity, confirming their essential roles in HS-mediated attachment.

Evidence 1Source 1DOI PubMedprovenance

Supporting Sources

Source 1primary paper2026MEDDOI PubMed

1 evidence snippet 3 linked claims Claim 1 Claim 2 Claim 3

Linked Claims

Claim 1engineering conclusionsupports2026Source 1DOI PubMed

Residue-level structure-guided engineering can enhance PFV transduction efficiency and helps define structural determinants of heparan sulfate recognition.

Quoted textsource-backed

These findings define the structural determinants of HS recognition in PFV Env and demonstrate that residue-level, structure-guided engineering can enhance PFV transduction efficiency.

Claim 2mechanism structure functionsupports2026Source 1DOI PubMed

Specific upper-domain PFV Env residues R298, R440, and E446 are essential for heparan sulfate-mediated attachment because alanine substitution abolishes infectivity.

Quoted textsource-backed

Alanine substitutions at R298, R440, and E446 in the UD abolished infectivity, confirming their essential roles in HS-mediated attachment.

Claim 3negative comparisonsupports2026Source 1DOI PubMed

Interspecies domain replacement with simian foamy virus Env reduces infectivity, indicating that PFV-heparan sulfate interactions are context specific.

Quoted textsource-backed

Interspecies domain replacement with simian foamy virus Env reduced infectivity, underscoring the context-specific nature of PFV-HS interactions.